TAILIEUCHUNG - Báo cáo khoa học: Anaerobic sulfatase-maturating enzyme – A mechanistic link with glycyl radical-activating enzymes?

Sulfatases form a major group of enzymes present in prokaryotes and eukaryotes. This class of hydrolases is unique in requiring essential post-translational modification of a critical active-site cysteinyl or seryl residue to Ca-formylglycine (FGly). | Anaerobic sulfatase-maturating enzyme - A mechanistic link with glycyl radical-activating enzymes Alhosna Benjdia1 Sowmya Subramanian2 Jerome Leprince3 Hubert Vaudry3 Michael K. Johnson2 and Olivier Berteau1 1 INRA UMR1319 MICALIS Domaine de Vilvert Jouy-en-Josas France 2 Department of Chemistry and Center for Metalloenzyme Studies University of Georgia Athens GA USA 3 INSERM U413 IFRMP23 UA CNRS Universite de Rouen Mont-Saint-Aignan France Keywords iron-sulfur center radicalS-adenosyl-L-methionine AdoMet enzyme S-adenosyl-L-methionine sulfatase Correspondence O. Berteau INRA UMR1319 MICALIS Beit 440 Domaine de Vilvert F-78352 Jouy-en-Josas France Fax 33 1346 52462 Tel 33 1346 52308 E-mail Received 8 October 2009 revised 22 December 2009 accepted 8 February 2010 doi Sulfatases form a major group of enzymes present in prokaryotes and eukaryotes. This class of hydrolases is unique in requiring essential post-translational modification of a critical active-site cysteinyl or seryl residue to Ca-formylglycine FGly . Herein we report mechanistic investigations of a unique class of radical-S-adenosyl-L-methionine AdoMet enzymes namely anaerobic sulfatase-maturating enzymes anSMEs which catalyze the oxidation of Cys-type and Ser-type sulfatases and possess three 4Fe-4S 2 clusters. We were able to develop a reliable quantitative enzymatic assay that allowed the direct measurement of FGly production and AdoMet cleavage. The results demonstrate stoichiometric coupling of AdoMet cleavage and FGly formation using peptide substrates with cysteinyl or seryl active-site residues. Analytical and EPR studies of the reconstituted wild-type enzyme and cysteinyl cluster mutants indicate the presence of three almost isopotential 4Fe-4S 2 clusters each of which is required for the generation of FGly in vitro. More surprisingly our data indicate that the two additional 4Fe-4S 2 clusters are required to obtain efficient .

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